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Database: UniProt
Entry: F2SEC4_TRIRC
LinkDB: F2SEC4_TRIRC
Original site: F2SEC4_TRIRC 
ID   F2SEC4_TRIRC            Unreviewed;       520 AA.
AC   F2SEC4;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   13-SEP-2023, entry version 55.
DE   RecName: Full=phosphoglycerate mutase (2,3-diphosphoglycerate-independent) {ECO:0000256|ARBA:ARBA00012026};
DE            EC=5.4.2.12 {ECO:0000256|ARBA:ARBA00012026};
GN   ORFNames=TERG_00974 {ECO:0000313|EMBL:EGD84697.1};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD84697.1, ECO:0000313|Proteomes:UP000008864};
RN   [1] {ECO:0000313|Proteomes:UP000008864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|ARBA:ARBA00004798}.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. {ECO:0000256|ARBA:ARBA00008819}.
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DR   EMBL; GG700648; EGD84697.1; -; Genomic_DNA.
DR   RefSeq; XP_003238988.1; XM_003238940.1.
DR   AlphaFoldDB; F2SEC4; -.
DR   STRING; 559305.F2SEC4; -.
DR   GeneID; 10375260; -.
DR   VEuPathDB; FungiDB:TERG_00974; -.
DR   eggNOG; KOG4513; Eukaryota.
DR   HOGENOM; CLU_026099_2_0_1; -.
DR   InParanoid; F2SEC4; -.
DR   OMA; FMDGRDT; -.
DR   OrthoDB; 212at2759; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000008864; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16010; iPGM; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   Gene3D; 3.40.1450.10; BPG-independent phosphoglycerate mutase, domain B; 1.
DR   HAMAP; MF_01038; GpmI; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR011258; BPG-indep_PGM_N.
DR   InterPro; IPR006124; Metalloenzyme.
DR   InterPro; IPR036646; PGAM_B_sf.
DR   InterPro; IPR005995; Pgm_bpd_ind.
DR   NCBIfam; TIGR01307; pgm_bpd_ind; 1.
DR   PANTHER; PTHR31637; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR31637:SF0; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR   Pfam; PF06415; iPGM_N; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   PIRSF; PIRSF001492; IPGAM; 1.
DR   SUPFAM; SSF64158; 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR001492-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001492-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008864}.
FT   DOMAIN          7..506
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
FT   DOMAIN          92..304
FT                   /note="BPG-independent PGAM N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06415"
FT   ACT_SITE        72
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-1"
FT   BINDING         14
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         72
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         163..164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         267..270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         341
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         408
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         412
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         449
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         450
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         467
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
SQ   SEQUENCE   520 AA;  56870 MW;  66C377AAE45E7351 CRC64;
     MAKVENKAVL IVIDGWGIPG PDSPKDGDAI AAAETPVMSG FAQEGSKTAQ GYTEIDASST
     AVGLPEGLMG NSEVGHLNIG AGRVVWQDVV RIDQTLKKGQ LGKVENIVKS FENAKNGNGR
     LHLLGLISDG GVHSHINHLF GLLQVAKDMG VPKVFIHFFG DGRDTDPKSA AGYMEKLLQK
     TQELGVGELA TVVGRYYAMD RDKRWDRIEV AMKGIVTGEG EESHDAVKTI KERYDKGEND
     EFLKPIIFGG QERRVQDNDT LFFFNYRSDR VREITQLLGD VDRSPKPDFP YPKSISITTM
     TRYKTDYTFP IAFAPQHMGN VLAEWLSKKQ LKQCHIAETE KYAHVTFFFN GGVEKQFEGE
     DREMIPSPKV ATYDLDPKMS AKPVGEKLAE RIADGKYEFL MNNFAPPDMV GHTGVYEAAI
     KGVAATDAAI GCVYEACKKH GYILFVTADH GNAEEMKNAD GTPKTSHTTN FVPFVMANAP
     EGWSLKKSGG VLGDVAPTVL AAMGIEQPEE MDGTSLLVKA
//
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